NES_SOYBN
ID NES_SOYBN Reviewed; 534 AA.
AC I1M2G5; R4HEK6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Neryl diphosphate diphosphatase, chloroplastic {ECO:0000305};
DE EC=3.7.1.27 {ECO:0000269|PubMed:24124526};
DE AltName: Full=Nerol synthase {ECO:0000303|PubMed:24124526};
DE Short=GmNES {ECO:0000303|PubMed:24124526};
GN Name=NES {ECO:0000303|PubMed:24124526};
GN ORFNames=GLYMA_13G250400 {ECO:0000312|EMBL:KRH21637.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=24124526; DOI=10.1371/journal.pone.0075972;
RA Zhang M., Liu J., Li K., Yu D.;
RT "Identification and characterization of a novel monoterpene synthase from
RT soybean restricted to neryl diphosphate precursor.";
RL PLoS ONE 8:e75972-e75972(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the hydrolysis of neryl
CC diphosphate (NPP) to form nerol and diphosphate (PubMed:24124526). Is
CC specific for NPP and has no hydrolase activity toward geranyl
CC diphosphate (GPP) or farnesyl diphosphate (FPP) (PubMed:24124526). The
CC monoterpene nerol may have an insect repellent effect for the plant
CC leaves (PubMed:24124526). {ECO:0000269|PubMed:24124526}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neryl diphosphate = diphosphate + nerol;
CC Xref=Rhea:RHEA:65828, ChEBI:CHEBI:15377, ChEBI:CHEBI:29452,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57665; EC=3.7.1.27;
CC Evidence={ECO:0000269|PubMed:24124526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65829;
CC Evidence={ECO:0000269|PubMed:24124526};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:24124526}.
CC -!- INDUCTION: Induced by salicylic acid (SA), wounding, and after feeding
CC by cotton leafworm (Spodoptera litura) larvae.
CC {ECO:0000269|PubMed:24124526}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: The growth and development of cotton leafworm was
CC retarded when feeding on NES-overexpressing tobacco leaves.
CC {ECO:0000269|PubMed:24124526}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JF758895; AEE92791.1; -; mRNA.
DR EMBL; CM000846; KRH21637.1; -; Genomic_DNA.
DR RefSeq; NP_001276223.1; NM_001289294.1.
DR AlphaFoldDB; I1M2G5; -.
DR SMR; I1M2G5; -.
DR STRING; 3847.GLYMA13G32380.1; -.
DR PRIDE; I1M2G5; -.
DR EnsemblPlants; KRH21637; KRH21637; GLYMA_13G250400.
DR Gramene; KRH21637; KRH21637; GLYMA_13G250400.
DR KEGG; gmx:100789381; -.
DR eggNOG; ENOG502QTGK; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR InParanoid; I1M2G5; -.
DR OMA; FMAKNFL; -.
DR OrthoDB; 449049at2759; -.
DR BioCyc; MetaCyc:MON-21312; -.
DR BRENDA; 3.7.1.27; 2483.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000008827; Chromosome 13.
DR ExpressionAtlas; I1M2G5; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Magnesium; Metal-binding; Plant defense; Plastid;
KW Reference proteome.
FT CHAIN 1..534
FT /note="Neryl diphosphate diphosphatase, chloroplastic"
FT /id="PRO_0000454898"
FT MOTIF 272..276
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 416
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 325
FT /note="Y -> C (in Ref. 1; AEE92791)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="E -> G (in Ref. 1; AEE92791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 62338 MW; 740B259761C60FA9 CRC64;
MDNIYIKQAL VLKEVKHVFQ KLIGEDPMES MYMVDTIQRL GIEHHFEEEI EAALQKQHLI
FSSHLSDFAN NHKLCEVALP FRLLRQRGHY VLADVFDNLK SNKKEFREKH GEDVKGLISL
YEATQLGIEG EDSLDDAGYL CHQLLHAWLT RHEEHNEAMY VAKTLQHPLH YDLSRFRDDT
SILLNDFKTK REWECLEELA EINSSIVRFV NQNEITQVYK WWKDLGLNNE VKFARYQPLK
WYMWPMACFT DPRFSEQRIE LTKPISLVYI IDDIFDVYGT LDQLTLFTDA IKRWELASTE
QLPDFMKMCL RVLYEITNDF AEKIYKKHGF NPIETLKRSW VRLLNAFLEE AHWLNSGHLP
RSAEYLNNGI VSTGVHVVLV HSFFLMDYSI NNEIVAIVDN VPQIIHSVAK ILRLSDDLEG
AKSEDQNGLD GSYIDCYMNE HQDVSAEDAQ RHVAHLISCE WKRLNREILT QNQLPSSFTN
FCLNAARMVP LMYHYRSNPG LSTLQEHVKL LSNNAVAGAE RHVVHILCLQ FVIE
